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- PDB-6g2a: Human [protein ADP-ribosylargenine] hydrolase ARH1 in complex wit... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6g2a | ||||||
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Title | Human [protein ADP-ribosylargenine] hydrolase ARH1 in complex with ADP-HPM | ||||||
![]() | [Protein ADP-ribosylarginine] hydrolase | ||||||
![]() | HYDROLASE / ADP-ribosylation / ADP-ribose / ADPRH / ADP-ribosylhydrolase / ARH1 / ADP-HPM | ||||||
Function / homology | ![]() [protein ADP-ribosylarginine] hydrolase / ADP-ribosylarginine hydrolase activity / protein de-ADP-ribosylation / potassium ion binding / protein modification process / magnesium ion binding / extracellular space Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Ariza, A. | ||||||
Funding support | ![]()
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![]() | ![]() Title: (ADP-ribosyl)hydrolases: Structural Basis for Differential Substrate Recognition and Inhibition. Authors: Rack, J.G.M. / Ariza, A. / Drown, B.S. / Henfrey, C. / Bartlett, E. / Shirai, T. / Hergenrother, P.J. / Ahel, I. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 164.6 KB | Display | ![]() |
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PDB format | ![]() | 128.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 740.1 KB | Display | ![]() |
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Full document | ![]() | 741.6 KB | Display | |
Data in XML | ![]() | 16.4 KB | Display | |
Data in CIF | ![]() | 23.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6g1pC ![]() 6g1qC ![]() 6g28C ![]() 6hgzC ![]() 6hh3C ![]() 6hh4C ![]() 6hh5C ![]() 6hh6C ![]() 6hozC ![]() 3hfwS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
-Protein , 1 types, 1 molecules A
#1: Protein | [ Mass: 40684.789 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P54922, [protein ADP-ribosylarginine] hydrolase |
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-Non-polymers , 5 types, 139 molecules ![](data/chem/img/A3R.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/ACT.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/ACT.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-A3R / | ||||||
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#3: Chemical | #4: Chemical | ChemComp-CL / | #5: Chemical | #6: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.04 Å3/Da / Density % sol: 39.67 % |
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Crystal grow | Temperature: 293.15 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 100 mM magnesium acetate, 12 % (w/v) PEG8000, 100 mM MOPS pH 7.5 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Jan 13, 2018 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0036 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→78.09 Å / Num. obs: 30388 / % possible obs: 99.4 % / Redundancy: 6.4 % / CC1/2: 0.999 / Rmerge(I) obs: 0.07 / Rpim(I) all: 0.044 / Rrim(I) all: 0.083 / Net I/σ(I): 12.8 |
Reflection shell | Resolution: 1.8→1.84 Å / Redundancy: 5 % / Rmerge(I) obs: 0.488 / Mean I/σ(I) obs: 2.7 / Num. unique obs: 1774 / CC1/2: 0.886 / Rpim(I) all: 0.302 / Rrim(I) all: 0.575 / % possible all: 99.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3HFW Resolution: 1.8→78.09 Å / Cor.coef. Fo:Fc: 0.964 / Cor.coef. Fo:Fc free: 0.949 / SU B: 8.14 / SU ML: 0.109 / Cross valid method: THROUGHOUT / ESU R: 0.141 / ESU R Free: 0.131 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 30.432 Å2
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Refinement step | Cycle: 1 / Resolution: 1.8→78.09 Å
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Refine LS restraints |
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